Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search General Information

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 28 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.18evolution OST is a heterooligomeric membrane protein complex in animals, plants, and fungi. In bacteria, archaea, and protozoa, OST is a monomer 720164
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.18evolution the catalytic subunit of OST is called STT3 in eukaryotes, AglB in archaea, and PglB in eubacteria. Archaeoglobus f ulgidus encodes three AglB paralogues, two of them are the shortest AglBs across all domains of life. -, 718929
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.18malfunction congenital disorders of glycosylation (CDG) have severe effects in humans, complete loss is lethal for eukaryots 707520
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.18malfunction defects in N-linked glycosylation results in a class of inherited diseases known as congenital disorders of glycosylation 758885
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.18malfunction instability of the temperature-sensitive DAD1 mutant at restrictive temperature causes a time-dependent degradation of the other OST subunits ribophorin I, ribophorin II, and OST48, disrupting the entire OST complex. Loss of OST activity caused by DAD1 instability results in severe hypoglycosylation that might induce apoptosis. Mutations affecting the biosynthesis of the activated Glc3Man9GlcNAc2 oligosaccharide substrate or the biogenesis of OSTs generally have a systemic effect in eukaryotes and alter glycosylation of many different glycoproteins 720164
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.18malfunction mutations affecting the biosynthesis of the activated Glc3Man9GlcNAc2 oligosaccharide substrate or the biogenesis of OSTs generally have a systemic effect in eukaryotes and alter glycosylation of many different glycoproteins 720164
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.18malfunction mutations affecting the biosynthesis of the activated Glc3Man9GlcNAc2 oligosaccharide substrate or the biogenesis of OSTs generally have a systemic effect in eukaryotes and alter glycosylation of many different glycoproteins. It is the substrate specificity of OST that translates defects in the biosynthesis of the oligosaccharide substrate into a generalized and multisystemic deficiency observed for the different forms of human congenital disorders of glycosylation type I. Mutations in the subunit paralogues N33/Tusc3 and IAP do not yield the pleiotropic phenotypes typical for CDG type I but specifically result in nonsyndromic mental retardation 720164
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.18malfunction simultaneous TbSTT3A and TbSTT3B knockdown prevents parasite growth in the bloodstream 708330
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.18metabolism in the central reaction of the N-linked glycosylation pathway, one of the most abundant modifications of proteins in eukaryotes, oligosaccharyltransferase, a multimeric complex located at the membrane of the endoplasmic reticulum, transfers a preassembled oligosaccharide to selected asparagine residues within the consensus sequence asparagine-X-serine/threonine 720164
Display the word mapDisplay the reaction diagram Show all sequences 2.4.99.18metabolism in the central reaction of the N-linked glycosylation pathway, one of the most abundant modifications of proteins in eukaryoties, oligosaccharyltransferase, a multimeric complex located at the membrane of the endoplasmic reticulum, transfers a preassembled oligosaccharide to selected asparagine residues within the consensus sequence asparagine-X-serine/threonine 720164
Results 1 - 10 of 28 > >>